ID A0A438B2M1_9NOCA Unreviewed; 584 AA.
AC A0A438B2M1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=EGT50_00770 {ECO:0000313|EMBL:RVW05201.1};
OS Rhodococcus xishaensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=2487364 {ECO:0000313|EMBL:RVW05201.1, ECO:0000313|Proteomes:UP000283479};
RN [1] {ECO:0000313|EMBL:RVW05201.1, ECO:0000313|Proteomes:UP000283479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LHW51113 {ECO:0000313|EMBL:RVW05201.1,
RC ECO:0000313|Proteomes:UP000283479};
RA Li L., Lin H.W.;
RT "Rhodococcus spongicola sp. nov. and Rhodococcus xishaensis sp. nov. from
RT marine sponges.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC Evidence={ECO:0000256|RuleBase:RU361217};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU361217};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC ECO:0000256|RuleBase:RU361217}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RVW05201.1}.
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DR EMBL; RKLO01000001; RVW05201.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A438B2M1; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000283479; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.8.870; Alpha-glycerophosphate oxidase, cap domain; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR031656; DAO_C.
DR InterPro; IPR038299; DAO_C_sf.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000447; G3P_DH_FAD-dep.
DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16901; DAO_C; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00977; FAD_G3PDH_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU361217};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217};
KW Reference proteome {ECO:0000313|Proteomes:UP000283479}.
FT DOMAIN 28..377
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 404..528
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 584 AA; 63292 MW; C5DAE468ACFDEE5B CRC64;
MDKQPGVQFL GPEQRERAWA QLGTEQFDVV VVGGGVVGAG AALDAATRGL KVALVEARDF
ASGTSSRSSK MFHGGLRYLE QLEFGLVAEA LRERELSMST LAPHLVKPLS FLFPLTHRVW
ERPYMAAGFL LYDRMGGAKS VPPQKHLTRA GALRMAPGLK RNALIGGIRF FDTVVDDARH
TMTVARTAAH YGTVVRTSTQ VVGFLREADR VSGVRVRDSE TGATTAVRGH VVINATGVWT
DEIQALSKQR GRFRVRASKG VHVVVPRDRI VSDSAIILRT ETSVLFVVPW GNHWIIGTTD
TDWNLDLAHP AATRADIDYI LGRVNTVLVT PLTYEDIDGV YAGLRPLLAG ESDETSKLSR
EHAVARVAPG LVAIAGGKYT TYRVMGRDAV DLAAEDIPAR VAPSITEKVP LAGADGYFAL
INQTVHLGAL HGLHPYRIKH LLDRYGSLID EVLDLADGSP ELLEPITEAP AYLQVEAVYA
AAAEGALHLE DMLARRTRIS IEYSHRGVDC AEQVARLMAR VLGWTEAEIV REVGNYRARV
EAEIMSQAQP DDASADALRA AAPEARAEIL EPVPGAVPSG SVRP
//
